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- W2183129599 abstract "pe ptone, 0.5; mannitol, 0.5; NaCl, 0.5; KCl, 1.0; CaCl2, 0.03 and MgSO4, 0.04 with pH 8, it produced 270 U protease mL -1 . The protease was partially purified by DEAE ion exchange and Sephadex G-75 gel filtration chromatography. The purified preparation contained two unseparated proteases with apparent molecular masses of 49 and 54 kDa, respectively. The preparation was stable at different concentrations of NaCl (0-15%, w/v) and pH range 6.0-12.0. It exhibited maximal activity at pH 7.5, temperature 50°C and 1% (w/v) NaCl. The Km and Vmax values towards casein were 7.5 mg mL -1 and 156.25 µg min -1 mL -1 , respectively. Inhibition of their proteolytic activity by EDTA and 1,10-phenanthroline indicated them to be metalloprotease in nature. The proteases exhibited remarkable stability in the presence of salt and organic solvents. These properties enable them for novel applications in non-aqueous enzymology and as an additive in detergent fo rmulations." @default.
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- W2183129599 date "2012-10-01" @default.
- W2183129599 modified "2023-09-24" @default.
- W2183129599 title "Isolation of a halophilic V irgibacillus sp. EMB13: Characterization of its protease for detergent application" @default.
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